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Use of electrospray ionization mass spectrometry to study binding interactions between subunits of DNA polvmerase III

Conference Paper


Abstract


  • The binding affinity between the TusTer protein-DNA complex involved in termination of DNA replication was investigated using electrospray ionization mass spectrometry (ESI-MS). The ε186-θ complex from DNA polymerase III was prepared for ESI-MS analysis by dialysis. The X-ray structure of the complex revealed substantial polar and electrostatic interactions between binding partners. The results show stability of ε186-θ complex to be >9 M in salt solutions suggesting that hydrophobic interactions play substantial role in stability of complex.

Publication Date


  • 2002

Citation


  • Gupta, R., Beck, J. L., Hamdan, S., Dixon, N. E., & Sheil, M. M. (2002). Use of electrospray ionization mass spectrometry to study binding interactions between subunits of DNA polvmerase III. In Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics (pp. 401-402).

Scopus Eid


  • 2-s2.0-2442641743

Web Of Science Accession Number


Start Page


  • 401

End Page


  • 402

Abstract


  • The binding affinity between the TusTer protein-DNA complex involved in termination of DNA replication was investigated using electrospray ionization mass spectrometry (ESI-MS). The ε186-θ complex from DNA polymerase III was prepared for ESI-MS analysis by dialysis. The X-ray structure of the complex revealed substantial polar and electrostatic interactions between binding partners. The results show stability of ε186-θ complex to be >9 M in salt solutions suggesting that hydrophobic interactions play substantial role in stability of complex.

Publication Date


  • 2002

Citation


  • Gupta, R., Beck, J. L., Hamdan, S., Dixon, N. E., & Sheil, M. M. (2002). Use of electrospray ionization mass spectrometry to study binding interactions between subunits of DNA polvmerase III. In Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics (pp. 401-402).

Scopus Eid


  • 2-s2.0-2442641743

Web Of Science Accession Number


Start Page


  • 401

End Page


  • 402